Neal Robert Melvin <nrmelvin at ucalgary.ca> wrote:
>I've been using Coomassie Blue staining to get a rough idea of the
>concentration of normal rabbit serum. When I do this, I notice that the
>bands corresponding to the heavy chains stain significantly more intensely
>than the light chain bands... should these be the rough the same intesity
>since one IgG contains 2 heavy chains and two light chains??
Im not familiar with Ig staining, but I think that generally staining
is dependent on protein mass. Thus, a protein with double molecular
weight than an other would give a stain that is twice intensive as the
stain of the other, given their molarity is equal.
However, staining intensity in fact depends on more factors, e.g.
amino acid composition. Furthermore, we used to do a lot of staining
with a protein that runs as a native trimer under standard
SDS-PAGE-conditions if the samples are not heated before applying onto
the gel, and as a usual denatured, SDS-bound monomer if heated. These
two species have a very different staining intensity although it's
chemically the same protein.
Bye, Frank
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